Dramatic improvement of crystal quality for low-temperature-grown rabbit muscle aldolase

作者：Park HaJeung; Rangarajan Erumbi S; Sygusch Jurgen^*; Izard Tina

来源：Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 2010, 66: 595-600.

DOI：10.1107/S1744309110011875

Rabbit muscle aldolase (RMA) was crystallized in complex with the low-complexity domain (LC4) of sorting nexin 9. Monoclinic crystals were obtained at room temperature that displayed large mosaicity and poor X-ray diffraction. However, orthorhombic RMA-LC4 crystals grown at 277 K under similar conditions exhibited low mosaicity, allowing data collection to 2.2 angstrom Bragg spacing and structure determination. It was concluded that the improvement of crystal quality as indicated by the higher resolution of the new RMA-LC4 complex crystals was a consequence of the introduction of new lattice contacts at lower temperature. The lattice contacts corresponded to an increased number of interactions between high-entropy side chains that mitigate the lattice strain incurred upon cryocooling and accompanying mosaic spread increases. The thermodynamically unfavorable immobilization of high-entropy side chains used in lattice formation was compensated by an entropic increase in the bulk-solvent content owing to the greater solvent content of the crystal lattice.

• 出版日期2010-5